› 1nba

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1nba/pdb
PDB entry 1nba coloured by chain, front view.
PDB entry 1nba coloured by chain, side view.
PDB entry 1nba coloured by chain, top view.
Source organism: Arthrobacter sp.
Primary publication:
Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution.
Romão MJ, Turk D, Gomis-Rüth FX, Huber R, Schumacher G, Möllering H, Rüssmann L
J Mol Biol 226 1111-30 (1992)
PMID: 1381445

Function and Biology Details

Reaction catalysed: 
N-carbamoylsarcosine + H(2)O = sarcosine + CO(2) + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-carbamoylsarcosine amidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 264 amino acids
Theoretical weight: 29.08 KDa
Source organism: Arthrobacter sp.
Expression system: Not provided
UniProt:
  • Canonical: P32400 (Residues: 1-264; Coverage: 100%)
Sequence domains: Isochorismatase family
Structure domains: Isochorismatase-like

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 136.22Å b: 122.29Å c: 70.87Å
α: 90° β: 91.82° γ: 90°
R-values:
R R work R free
0.186 0.186 not available
Expression system: Not provided

Quick links

Citations

4 review citations

Creatine and creatinine metabolism.
Wyss et al. (2000)
3 more

12 mentions without citation

Molecular replacement: tricks and treats.
Abergel C. (2013)
11 more